TAL_THET8
ID TAL_THET8 Reviewed; 223 AA.
AC Q5SJE8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Probable transaldolase {ECO:0000255|HAMAP-Rule:MF_00494};
DE EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00494};
GN Name=tal {ECO:0000255|HAMAP-Rule:MF_00494}; OrderedLocusNames=TTHA1066;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_00494}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00494};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage):
CC step 2/3. {ECO:0000255|HAMAP-Rule:MF_00494}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00494}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00494}.
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DR EMBL; AP008226; BAD70889.1; -; Genomic_DNA.
DR RefSeq; WP_011228415.1; NC_006461.1.
DR RefSeq; YP_144332.1; NC_006461.1.
DR PDB; 1WX0; X-ray; 2.27 A; A/B/C/D/E/F/G/H/I/J=1-223.
DR PDBsum; 1WX0; -.
DR AlphaFoldDB; Q5SJE8; -.
DR SMR; Q5SJE8; -.
DR STRING; 300852.55772448; -.
DR EnsemblBacteria; BAD70889; BAD70889; BAD70889.
DR GeneID; 3168258; -.
DR KEGG; ttj:TTHA1066; -.
DR PATRIC; fig|300852.9.peg.1046; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_0_0_0; -.
DR OMA; VRHPMHV; -.
DR PhylomeDB; Q5SJE8; -.
DR UniPathway; UPA00115; UER00414.
DR EvolutionaryTrace; Q5SJE8; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00956; Transaldolase_FSA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR033919; TSA/FSA_arc/bac.
DR PANTHER; PTHR10683; PTHR10683; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Pentose shunt; Reference proteome; Schiff base;
KW Transferase.
FT CHAIN 1..223
FT /note="Probable transaldolase"
FT /id="PRO_1000126370"
FT ACT_SITE 92
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00494"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1WX0"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:1WX0"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:1WX0"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:1WX0"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:1WX0"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:1WX0"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 177..185
FT /evidence="ECO:0007829|PDB:1WX0"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:1WX0"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:1WX0"
SQ SEQUENCE 223 AA; 24023 MW; F5C9D213FB1E2E47 CRC64;
MELYLDTASL EEIREIAAWG VLSGVTTNPT LVAKAFAAKG EALTEEAFAA HLRAICETVG
GPVSAEVTAL EAEAMVAEGR RLAAIHPNIV VKLPTTEEGL KACKRLSAEG IKVNMTLIFS
ANQALLAARA GASYVSPFLG RVDDISWDGG ELLREIVEMI QVQDLPVKVI AASIRHPRHV
TEAALLGADI ATMPHAVFKQ LLKHPLTDIG LKRFLEDWEK VKP
